{"title":"Role of ceruloplasmin as a low grade chronic inflammatory marker and activated innate immune system in pathogenesis of diabetes mellitus","authors":"S. Mohiuddin, P. Manjrekar","doi":"10.15406/JDMDC.2018.05.00155","DOIUrl":null,"url":null,"abstract":"Ceruloplasmin is one the important components of the multicopper oxidase family of enzymes. Three types of spectroscopically distinct copper sites are present in this evolutionarily conserved group of proteins.1 The signature sequences encompassing the amino acid ligands for copper are highly conserved among all multicopper oxidases. The substrates, the number of type I coppers and precise mechanism of intramolecular electron transfer differ from protein to protein.2 Unique members of this family of enzymes, which include the well characterized protein laccase and ascorbate oxidase, are present in bacteria, fungi, yeast, plants, worms, parasites and mammals. Manganese, iron, nitrate, bilirubin, phenol and ascorbate are the known substrates of the multicopper oxidase.2","PeriodicalId":92240,"journal":{"name":"Journal of diabetes, metabolic disorders & control","volume":"62 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2018-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of diabetes, metabolic disorders & control","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15406/JDMDC.2018.05.00155","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5
Abstract
Ceruloplasmin is one the important components of the multicopper oxidase family of enzymes. Three types of spectroscopically distinct copper sites are present in this evolutionarily conserved group of proteins.1 The signature sequences encompassing the amino acid ligands for copper are highly conserved among all multicopper oxidases. The substrates, the number of type I coppers and precise mechanism of intramolecular electron transfer differ from protein to protein.2 Unique members of this family of enzymes, which include the well characterized protein laccase and ascorbate oxidase, are present in bacteria, fungi, yeast, plants, worms, parasites and mammals. Manganese, iron, nitrate, bilirubin, phenol and ascorbate are the known substrates of the multicopper oxidase.2
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